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A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a glycolytic enzyme, catalyses the conversion of d-glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate. While mammalian and yeast GAPDHs are multifunctional proteins that have additional functions beyond those involved in glycolysis, including rea...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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International Union of Crystallography
2018
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5931139/ https://www.ncbi.nlm.nih.gov/pubmed/29717994 http://dx.doi.org/10.1107/S2053230X18004557 |
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author | Kim, Yong Ju |
author_facet | Kim, Yong Ju |
author_sort | Kim, Yong Ju |
collection | PubMed |
description | Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a glycolytic enzyme, catalyses the conversion of d-glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate. While mammalian and yeast GAPDHs are multifunctional proteins that have additional functions beyond those involved in glycolysis, including reactions related to nuclear RNA transport, DNA replication/repair, membrane fusion and cellular apoptosis, Escherichia coli GAPDH (ecGAPDH) has only been reported to function in glycolysis. The S-loop of GAPDH is required for interaction with its cofactor and with other proteins. In this study, the three-dimensional crystal structure of GAPDH treated with trehalose is reported at 2.0 Å resolution. Trehalose was used as a cryoprotectant for the GAPDH crystals. The structure of trehalose-bound ecGAPDH was compared with the structures of both NAD(+)-free and NAD(+)-bound ecGAPDH. At the S-loop, the bound trehalose in the GAPDH structure induces a 2.4° rotation compared with the NAD(+)-free ecGAPDH structure and a 3.1° rotation compared with the NAD(+)-bound ecGAPDH structure. |
format | Online Article Text |
id | pubmed-5931139 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-59311392018-05-11 A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase Kim, Yong Ju Acta Crystallogr F Struct Biol Commun Research Communications Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a glycolytic enzyme, catalyses the conversion of d-glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate. While mammalian and yeast GAPDHs are multifunctional proteins that have additional functions beyond those involved in glycolysis, including reactions related to nuclear RNA transport, DNA replication/repair, membrane fusion and cellular apoptosis, Escherichia coli GAPDH (ecGAPDH) has only been reported to function in glycolysis. The S-loop of GAPDH is required for interaction with its cofactor and with other proteins. In this study, the three-dimensional crystal structure of GAPDH treated with trehalose is reported at 2.0 Å resolution. Trehalose was used as a cryoprotectant for the GAPDH crystals. The structure of trehalose-bound ecGAPDH was compared with the structures of both NAD(+)-free and NAD(+)-bound ecGAPDH. At the S-loop, the bound trehalose in the GAPDH structure induces a 2.4° rotation compared with the NAD(+)-free ecGAPDH structure and a 3.1° rotation compared with the NAD(+)-bound ecGAPDH structure. International Union of Crystallography 2018-04-16 /pmc/articles/PMC5931139/ /pubmed/29717994 http://dx.doi.org/10.1107/S2053230X18004557 Text en © Kim 2018 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/2.0/uk/ |
spellingShingle | Research Communications Kim, Yong Ju A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase |
title | A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase |
title_full | A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase |
title_fullStr | A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase |
title_full_unstemmed | A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase |
title_short | A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase |
title_sort | cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase |
topic | Research Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5931139/ https://www.ncbi.nlm.nih.gov/pubmed/29717994 http://dx.doi.org/10.1107/S2053230X18004557 |
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